2f52
From Proteopedia
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Solution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine
Overview
Cold shock proteins (CSP) belong to the family of single-stranded nucleic, acid binding proteins with OB-fold. CSP are believed to function as 'RNA, chaperones' and during anti-termination. We determined the solution, structure of Bs-CspB bound to the single-stranded DNA (ssDNA) fragment, heptathymidine (dT7) by NMR spectroscopy. Bs-CspB reveals an almost, invariant conformation when bound to dT7 with only minor reorientations in, loop beta1-beta2 and beta3-beta4 and of few aromatic side chains involved, in base stacking. Binding studies of protein variants and mutated ssDNA, demonstrated that Bs-CspB associates with ssDNA at almost diffusion, controlled rates and low sequence specificity consistent with its, biological function. A variation of the ssDNA affinity is accomplished, solely by changes of the dissociation rate. 15N NMR relaxation and H/D, exchange experiments revealed that binding of dT7 increases the stability, of Bs-CspB and reduces the sub-nanosecond dynamics of the entire protein, and especially of loop beta3-beta4.
About this Structure
2F52 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution., Zeeb M, Max KE, Weininger U, Low C, Sticht H, Balbach J, Nucleic Acids Res. 2006;34(16):4561-71. Epub 2006 Sep 6. PMID:16956971
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